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Database: UniProt
Entry: A0A1M5AY15_9BACT
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ID   A0A1M5AY15_9BACT        Unreviewed;       424 AA.
AC   A0A1M5AY15;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000256|RuleBase:RU004136};
DE            EC=6.3.2.10 {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000256|RuleBase:RU004136};
DE   AltName: Full=D-alanyl-D-alanine-adding enzyme {ECO:0000256|HAMAP-Rule:MF_02019};
GN   Name=murF {ECO:0000256|HAMAP-Rule:MF_02019};
GN   ORFNames=SAMN02745131_02401 {ECO:0000313|EMBL:SHF35128.1};
OS   Flavisolibacter ginsengisoli DSM 18119.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Flavisolibacter.
OX   NCBI_TaxID=1121884 {ECO:0000313|EMBL:SHF35128.1, ECO:0000313|Proteomes:UP000184048};
RN   [1] {ECO:0000313|EMBL:SHF35128.1, ECO:0000313|Proteomes:UP000184048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18119 {ECO:0000313|EMBL:SHF35128.1,
RC   ECO:0000313|Proteomes:UP000184048};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in cell wall formation. Catalyzes the final step in
CC       the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of
CC       murein. {ECO:0000256|HAMAP-Rule:MF_02019,
CC       ECO:0000256|RuleBase:RU004136}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-
CC         alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate = ADP + H(+) +
CC         phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-
CC         meso-2,6-diaminopimeloyl-D-alanyl-D-alanine; Xref=Rhea:RHEA:28374,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57822, ChEBI:CHEBI:61386, ChEBI:CHEBI:83905,
CC         ChEBI:CHEBI:456216; EC=6.3.2.10; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02019, ECO:0000256|RuleBase:RU004136};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000256|RuleBase:RU004136}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02019,
CC       ECO:0000256|RuleBase:RU004136}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. MurF subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_02019}.
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DR   EMBL; FQUU01000009; SHF35128.1; -; Genomic_DNA.
DR   RefSeq; WP_072835569.1; NZ_FQUU01000009.1.
DR   AlphaFoldDB; A0A1M5AY15; -.
DR   STRING; 1121884.SAMN02745131_02401; -.
DR   OrthoDB; 9801978at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000184048; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0047480; F:UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008766; F:UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate-D-alanyl-D-alanine ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR   Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR   Gene3D; 3.40.1390.10; MurE/MurF, N-terminal domain; 1.
DR   HAMAP; MF_02019; MurF; 1.
DR   InterPro; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR000713; Mur_ligase_N.
DR   InterPro; IPR035911; MurE/MurF_N.
DR   InterPro; IPR005863; UDP-N-AcMur_synth.
DR   NCBIfam; TIGR01143; murF; 1.
DR   PANTHER; PTHR43024; UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE; 1.
DR   PANTHER; PTHR43024:SF1; UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE; 1.
DR   Pfam; PF01225; Mur_ligase; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR   SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR   SUPFAM; SSF63418; MurE/MurF N-terminal domain; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02019};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW   Rule:MF_02019};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW   Rule:MF_02019};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW   Rule:MF_02019};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|HAMAP-Rule:MF_02019};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02019};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_02019, ECO:0000313|EMBL:SHF35128.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02019};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW   Rule:MF_02019}; Reference proteome {ECO:0000313|Proteomes:UP000184048}.
FT   DOMAIN          16..83
FT                   /note="Mur ligase N-terminal catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01225"
FT   DOMAIN          94..276
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
FT   DOMAIN          300..377
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
FT   BINDING         96..102
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02019"
SQ   SEQUENCE   424 AA;  47194 MW;  073AB41D7EE76905 CRC64;
     MNIEELYTLY LQNPSIQTDT RKLKKGDLFF ALKGPSFNGN EFAAKAIDAG ASYVIIDDPK
     YAMDRTIVVG DVLKTLQELA RHHRLQFDIP FIAITGSNGK TTTKELIHAV LSSSFTTYTT
     EGNLNNHIGV PLTILKIRKD AQMAVIEMGA NHQKEIDSYC QYAMPTHGLI TNVGKAHLEG
     FGGEEGVKKG KGELFDYLRQ HKGTVFIMSD YDYLQEMSKG IPVVYTYGTK EAQVTGNIYQ
     TDPFVAVQFS KGYEGIIQTH LVGSYNLPNI LSAVAIGHYF KVPPGKIRAA IESYMPSNSR
     SQLMQKGNNQ IILDAYNANP SSMKAAIENF GSMKADDKVL ALGAMAELGT SSIKEHEMLI
     EQIQKYPWKD VILVGGDFMQ IKHPFHQFTS SKEAGEWMKG KYKNACLLIK GSRSIQMEKV
     LDYL
//
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